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P03188

- GB_EBVB9

UniProt

P03188 - GB_EBVB9

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Protein
Envelope glycoprotein B
Gene
gB, BALF4
Organism
Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Envelope glycoprotein that forms spikes at the surface of virion envelope. Involved in fusion of viral and cellular membranes leading to virus entry into the host cell. Following initial binding of gp350/220 to its receptor, membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. May also be involved in the fusion between the virion envelope and the outer nuclear membrane during virion morphogenesis By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei432 – 4332Cleavage; by host furin Reviewed prediction

Names & Taxonomyi

Protein namesi
Recommended name:
Envelope glycoprotein B
Short name:
gB
Alternative name(s):
GP115
Glycoprotein GP110
Gene namesi
Name:gB
ORF Names:BALF4
OrganismiEpstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Taxonomic identifieri10377 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeGammaherpesvirinaeLymphocryptovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000007640: Genome

Subcellular locationi

Virion membrane; Single-pass type I membrane protein By similarity. Host cell membrane; Single-pass type I membrane protein By similarity. Host endosome membrane; Single-pass type I membrane protein By similarity. Host Golgi apparatus membrane; Single-pass type I membrane protein By similarity
Note: During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN) By similarity.1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 732710Virion surface Reviewed prediction
Add
BLAST
Transmembranei733 – 75321Helical; Reviewed prediction
Add
BLAST
Topological domaini754 – 857104Intravirion Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. host cell Golgi membrane Source: UniProtKB-SubCell
  2. host cell endosome membrane Source: UniProtKB-SubCell
  3. host cell plasma membrane Source: UniProtKB-SubCell
  4. integral component of membrane Source: UniProtKB-KW
  5. viral envelope Source: UniProtKB-KW
  6. virion membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host endosome, Host Golgi apparatus, Host membrane, Membrane, Viral envelope protein, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi112 – 1132WY → HR: Loss of fusion with epithelial cells.
Mutagenesisi193 – 1964WLIW → RVEA: Loss of fusion with epithelial cells. 1 Publication
Mutagenesisi428 – 4325RRRRR → DDDDK: Complete loss of proteolytic cleavage. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222 Reviewed prediction
Add
BLAST
Chaini23 – 857835Envelope glycoprotein B
PRO_0000038190Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi51 ↔ 528
Disulfide bondi68 ↔ 484
Glycosylationi76 – 761N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi141 ↔ 206
Glycosylationi163 – 1631N-linked (GlcNAc...); by host1 Publication
Glycosylationi290 – 2901N-linked (GlcNAc...); by host1 Publication
Disulfide bondi295 ↔ 342
Glycosylationi329 – 3291N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi348 – 3481N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi395 – 3951N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi436 – 4361N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi551 ↔ 588 By similarity
Glycosylationi563 – 5631N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi629 – 6291N-linked (GlcNAc...); by host1 Publication

Post-translational modificationi

A proteolytic cleavage by host furin generates two subunits that remain linked by disulfide bonds Inferred.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotrimer; disulfide-linked By similarity.1 Publication

Protein-protein interaction databases

DIPiDIP-47669N.
MINTiMINT-6768112.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi58 – 603
Beta strandi77 – 8711
Beta strandi92 – 11019
Beta strandi115 – 12511
Helixi129 – 1357
Turni136 – 1383
Beta strandi140 – 14910
Beta strandi152 – 1576
Helixi158 – 1603
Beta strandi165 – 1673
Beta strandi179 – 1835
Beta strandi197 – 21519
Beta strandi222 – 2243
Beta strandi229 – 2324
Turni248 – 2503
Beta strandi251 – 2577
Helixi262 – 2643
Beta strandi272 – 2787
Beta strandi283 – 2875
Helixi291 – 2933
Beta strandi296 – 31015
Beta strandi315 – 3195
Turni320 – 3234
Beta strandi324 – 3296
Helixi341 – 3433
Helixi344 – 35613
Turni357 – 3615
Beta strandi362 – 3687
Beta strandi370 – 3745
Beta strandi379 – 3879
Helixi458 – 49841
Helixi502 – 5109
Beta strandi516 – 5194
Beta strandi522 – 5254
Beta strandi533 – 5386
Beta strandi556 – 5605
Beta strandi567 – 5726
Beta strandi576 – 5794
Beta strandi593 – 5986
Beta strandi601 – 6066
Beta strandi609 – 6157
Turni616 – 6183
Helixi646 – 6505
Helixi657 – 67317

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FVCX-ray3.20A23-685[»]
ProteinModelPortaliP03188.

Miscellaneous databases

EvolutionaryTraceiP03188.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni111 – 1144Involved in fusion and/or binding to host membrane Reviewed prediction
Regioni193 – 1975Involved in fusion and/or binding to host membrane Reviewed prediction
Regioni561 – 62060Oligomerization
Add
BLAST
Regioni709 – 72921Hydrophobic membrane proximal region
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi428 – 4325Poly-Arg
Compositional biasi836 – 8394Poly-Arg

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Family and domain databases

InterProiIPR000234. Herpes_Glycoprot_B.
[Graphical view]
PfamiPF00606. Glycoprotein_B. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P03188-1 [UniParc]FASTAAdd to Basket

« Hide

MTRRRVLSVV VLLAALACRL GAQTPEQPAP PATTVQPTAT RQQTSFPFRV    50
CELSSHGDLF RFSSDIQCPS FGTRENHTEG LLMVFKDNII PYSFKVRSYT 100
KIVTNILIYN GWYADSVTNR HEEKFSVDSY ETDQMDTIYQ CYNAVKMTKD 150
GLTRVYVDRD GVNITVNLKP TGGLANGVRR YASQTELYDA PGWLIWTYRT 200
RTTVNCLITD MMAKSNSPFD FFVTTTGQTV EMSPFYDGKN KETFHERADS 250
FHVRTNYKIV DYDNRGTNPQ GERRAFLDKG TYTLSWKLEN RTAYCPLQHW 300
QTFDSTIATE TGKSIHFVTD EGTSSFVTNT TVGIELPDAF KCIEEQVNKT 350
MHEKYEAVQD RYTKGQEAIT YFITSGGLLL AWLPLTPRSL ATVKNLTELT 400
TPTSSPPSSP SPPAPSAARG STPAAVLRRR RRDAGNATTP VPPTAPGKSL 450
GTLNNPATVQ IQFAYDSLRR QINRMLGDLA RAWCLEQKRQ NMVLRELTKI 500
NPTTVMSSIY GKAVAAKRLG DVISVSQCVP VNQATVTLRK SMRVPGSETM 550
CYSRPLVSFS FINDTKTYEG QLGTDNEIFL TKKMTEVCQA TSQYYFQSGN 600
EIHVYNDYHH FKTIELDGIA TLQTFISLNT SLIENIDFAS LELYSRDEQR 650
ASNVFDLEGI FREYNFQAQN IAGLRKDLDN AVSNGRNQFV DGLGELMDSL 700
GSVGQSITNL VSTVGGLFSS LVSGFISFFK NPFGGMLILV LVAGVVILVI 750
SLTRRTRQMS QQPVQMLYPG IDELAQQHAS GEGPGINPIS KTELQAIMLA 800
LHEQNQEQKR AAQRAAGPSV ASRALQAARD RFPGLRRRRY HDPETAAALL 850
GEAETEF 857
Length:857
Mass (Da):95,639
Last modified:July 21, 1986 - v1
Checksum:iD9BCE9487D8A1411
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
V01555 Genomic DNA. Translation: CAA24806.1.
AJ507799 Genomic DNA. Translation: CAD53463.1.
PIRiA03749. QQBE1L.
RefSeqiYP_401713.1. NC_007605.1.

Genome annotation databases

GeneIDi3783680.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
V01555 Genomic DNA. Translation: CAA24806.1 .
AJ507799 Genomic DNA. Translation: CAD53463.1 .
PIRi A03749. QQBE1L.
RefSeqi YP_401713.1. NC_007605.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3FVC X-ray 3.20 A 23-685 [» ]
ProteinModelPortali P03188.
ModBasei Search...

Protein-protein interaction databases

DIPi DIP-47669N.
MINTi MINT-6768112.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 3783680.

Miscellaneous databases

EvolutionaryTracei P03188.

Family and domain databases

InterProi IPR000234. Herpes_Glycoprot_B.
[Graphical view ]
Pfami PF00606. Glycoprotein_B. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis of the 17,166 base-pair EcoRI fragment C of B95-8 Epstein-Barr virus."
    Bankier A.T., Deininger P.L., Farrell P.J., Barrell B.G.
    Mol. Biol. Med. 1:21-45(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Epstein-Barr virus glycoprotein homologous to herpes simplex virus gB."
    Gong M., Ooka T., Matsuo T., Kieff E.
    J. Virol. 61:499-508(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF PROTEIN.
  4. Cited for: SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE.
  5. "Characterization of EBV gB indicates properties of both class I and class II viral fusion proteins."
    Backovic M., Leser G.P., Lamb R.A., Longnecker R., Jardetzky T.S.
    Virology 368:102-113(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF 112-TRP-TYR-113; 193-TRP--TRP-196 AND 428-ARG--ARG-432, PROTEOLYTIC CLEAVAGE.
  6. "Analysis of Epstein-Barr virus glycoprotein B functional domains via linker insertion mutagenesis."
    Reimer J.J., Backovic M., Deshpande C.G., Jardetzky T., Longnecker R.
    J. Virol. 83:734-747(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: OLIGOMERIZATION REGION.
  7. "Cleavage of Epstein-Barr virus glycoprotein B is required for full function in cell-cell fusion with both epithelial and B cells."
    Sorem J., Longnecker R.
    J. Gen. Virol. 90:591-595(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC CLEAVAGE BY HOST FURIN.
  8. "Structure of a trimeric variant of the Epstein-Barr virus glycoprotein B."
    Backovic M., Longnecker R., Jardetzky T.S.
    Proc. Natl. Acad. Sci. U.S.A. 106:2880-2885(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 23-685, GLYCOSYLATION AT ASN-163; ASN-290 AND ASN-629.

Entry informationi

Entry nameiGB_EBVB9
AccessioniPrimary (citable) accession number: P03188
Secondary accession number(s): Q777B0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 14, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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